EC Number   |
Protein Variants |
Reference |
|---|
   3.4.24.14 | more |
ADAMTS2 mutated at the furin-cleavage site separating the pro domain and the metalloprotease domain lacks enzymatic activity |
668857 |
| 3.4.24.14 | more |
generation of ADAMTS2-KO mice, phenotype, overview |
753779 |
| 3.4.24.14 | more |
in vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that can also involve direct anti-tumor effects |
734611 |
| 3.4.24.14 | more |
removal of the PNP domain, which significantly increases enzyme activity, removal of the fourth and the second TSPI repeats, which represses the enzymatic activity, no activity when lacking the central domain or mutated at the catalytic site, mutation of the potential cleavage site by furin strongly represses, but not abolishes enzyme activity, removal of adjacent domains completely suppresses activity, use of chimeric enzyme shows significant level of activity only when the metalloprotease domain or the other central domains are present, replacement of the C-terminal domains by GON-1 or ADAMTS-14 results in reduced activity |
669386 |
| 3.4.24.14 | more |
three constructs coding for catalytically inactive ADAMTS-2 or for ADAMTS-2 lacking either the central or the C-terminal domains are created and used for stable transfection of HEK 293-EBNA cells. Results show that the catalytic activity of ADAMTS-2 is dispensable for antiangiogenic activity |
717467 |
